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Stepwise protein-mediated RNA folding directs assembly of telomerase ribonucleoprotein

Author

Listed:
  • Michael D. Stone

    (Department of Chemistry and Chemical Biology,)

  • Mariana Mihalusova

    (Department of Molecular and Cellular Biology,)

  • Catherine M. O’Connor

    (University of California, Berkeley, California 94720, USA)

  • Ramadevi Prathapam

    (University of California, Berkeley, California 94720, USA)

  • Kathleen Collins

    (University of California, Berkeley, California 94720, USA)

  • Xiaowei Zhuang

    (Department of Chemistry and Chemical Biology,
    and
    Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts 02138, USA)

Abstract

How telomerase shapes up The biogenesis of telomerase, the ribonucleoprotein (RNP) assembly that stabilizes the termini of linear chromosomes, is an important process in a healthy cell and mutations that disrupt it cause disease. Mechanisms of RNP assembly are poorly understood. Michael Stone et al. have used a single-molecule approach to examine telomerase assembly in real time. The results establish an assembly mechanism featuring successive steps of protein-induced RNA folding, ultimately moulding the telomerase complex into its functional shape.

Suggested Citation

  • Michael D. Stone & Mariana Mihalusova & Catherine M. O’Connor & Ramadevi Prathapam & Kathleen Collins & Xiaowei Zhuang, 2007. "Stepwise protein-mediated RNA folding directs assembly of telomerase ribonucleoprotein," Nature, Nature, vol. 446(7134), pages 458-461, March.
    • Handle: RePEc:nat:nature:v:446:y:2007:i:7134:d:10.1038_nature05600
    DOI: 10.1038/nature05600
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    Cited by:

    1. Diego J. Páez-Moscoso & David V. Ho & Lili Pan & Katie Hildebrand & Kristi L. Jensen & Michaella J. Levy & Laurence Florens & Peter Baumann, 2022. "A putative cap binding protein and the methyl phosphate capping enzyme Bin3/MePCE function in telomerase biogenesis," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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